› 6gua

Hybrid

Xylulose 5-phosphate phosphoketolase from Lactococcus lactis

Released:
DOI: 10.2210/pdb6gua/pdb
PDB entry 6gua coloured by chain, front view.
PDB entry 6gua coloured by chain, side view.
PDB entry 6gua coloured by chain, top view.
Source organism: Lactococcus lactis subsp. lactis Il1403
Primary publication:
Crystal structure of a xylulose 5-phosphate phosphoketolase. Insights into the substrate specificity for xylulose 5-phosphate.
Scheidig AJ, Horvath D, Szedlacsek SE
J Struct Biol 207 85-102 (2019)
PMID: 31059775

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189960 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable phosphoketolase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 822 amino acids
Theoretical weight: 93.47 KDa
Source organism: Lactococcus lactis subsp. lactis Il1403
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9CFH4 (Residues: 1-822; Coverage: 100%)
Gene names: L138230, LL1502
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand TPP 8 x TPP
Ligand MG 8 x MG
Ligand PO4 8 x PO4
No modified residues

Experiments and Validation Details

Experimental Method: X-ray diffraction, X-ray solution scattering
X-ray source: ESRF BEAMLINE ID13
Spacegroup: P21
Unit cell:
a: 158.1Å b: 141.5Å c: 161.15Å
α: 90° β: 90.29° γ: 90°
R-values:
R R work R free
0.212 0.212 0.261
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

An ATP-sensitive phosphoketolase regulates carbon fixation in cyanobacteria.
Lu et al. (2023)
1 more

1 mention without citation

Structural basis for replication origin unwinding by an initiator primase of plasmid ColE2-P9: duplex DNA unwinding by a single protein.
Itou et al. (2015)